1myk: Difference between revisions

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[[Image:1myk.png|left|200px]]
==CRYSTAL STRUCTURE, FOLDING, AND OPERATOR BINDING OF THE HYPERSTABLE ARC REPRESSOR MUTANT PL8==
<StructureSection load='1myk' size='340' side='right' caption='[[1myk]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1myk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MYK FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MUTATED ARC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10754 Enterobacteria phage P22])</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1myk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1myk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1myk RCSB], [http://www.ebi.ac.uk/pdbsum/1myk PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Arc repressor is a small, dimeric DNA-binding protein that belongs to the ribbon-helix-helix family of transcription factors. Replacing Pro8 at the N-terminal end of the beta-sheet with leucine increases the stability of the mutant protein by 2.5 kcal/mol of dimer. However, this enhanced stability is achieved at the expense of significantly reduced DNA binding affinity. The structure of the PL8 mutant dimer has been determined to 2.4-A resolution by X-ray crystallography. The overall structure of the mutant is very similar to wild type, but Leu8 makes an additional interstrand hydrogen bond at each end of the beta-sheet of the mutant, increasing the total number of beta-sheet hydrogen bonds from six to eight. Comparison of the refolding and unfolding kinetics of the PL8 mutant and wild-type Arc shows that the enhanced stability of the mutant is accounted for by a decrease in the rate of protein unfolding, suggesting that the mutation acts to stabilize the native state and that the beta-sheet forms after the rate-limiting step in folding. The reduced operator affinity of the PL8 dimer appears to arise because the mutant cannot make the new interstrand hydrogen bonds and simultaneously make the wild-type set of contacts with operator DNA.


{{STRUCTURE_1myk|  PDB=1myk  |  SCENE=  }}
Crystal structure, folding, and operator binding of the hyperstable Arc repressor mutant PL8.,Schildbach JF, Milla ME, Jeffrey PD, Raumann BE, Sauer RT Biochemistry. 1995 Jan 31;34(4):1405-12. PMID:7827088<ref>PMID:7827088</ref>


===CRYSTAL STRUCTURE, FOLDING, AND OPERATOR BINDING OF THE HYPERSTABLE ARC REPRESSOR MUTANT PL8===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_7827088}}
 
==About this Structure==
[[1myk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p22 Enterobacteria phage p22]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYK OCA].


==See Also==
==See Also==
*[[Myosin|Myosin]]
*[[Myosin|Myosin]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:007827088</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Enterobacteria phage p22]]
[[Category: Enterobacteria phage p22]]
[[Category: Jeffrey, P D.]]
[[Category: Jeffrey, P D.]]
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